1zy6

Membrane-bound dimer structure of Protegrin-1 (PG-1), a beta-Hairpin Antimicrobial Peptide in Lipid Bilayers from Rotational-Echo Double-Resonance Solid-State NMR

spinqualitylabelsall models 1zy6 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1zy6 is a 2 chain structure with sequence from Sus scrofa. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solid-state NMR Ligands: NH2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PG1_PIG Microbicidal activity. Active against E.coli, Listeria monocytogenes and C.albicans, in vitro. Publication Abstract from PubMed The intermolecular packing of a beta-hairpin antimicrobial peptide, PG-1, in lipid bilayers is determined using solid-state NMR distance measurements. Previous spin counting experiments showed that PG-1 associates as dimers in POPC bilayers; however, the detailed dimer structure was unknown. We have now measured several intermolecular 13C-19F, 1H-13C, and 15N-13C distances in site-specifically labeled PG-1 to constrain the structure of the intermolecular interface. The distances are measured using the rotational-echo double-resonance (REDOR) technique under magic-angle spinning. The results indicate that two PG-1 molecules align in a parallel fashion with the C-terminal strand of the hairpin forming the dimer interface. Six hydrogen bonds stabilize this interface, and the Phe12 side chain adopts the g- conformation in the membrane as in solution. The parallel packing of the peptide in the lipid bilayer differs from the antiparallel dimer found in DPC micelles and may be stabilized by its strong amphipathic character, which should facilitate its insertion into the amphipathic lipid bilayer. This study demonstrates the utility of the REDOR NMR technique for the elucidation of the oligomeric structure of membrane proteins. Membrane-bound dimer structure of a beta-hairpin antimicrobial peptide from rotational-echo double-resonance solid-state NMR.,Mani R, Tang M, Wu X, Buffy JJ, Waring AJ, Sherman MA, Hong M Biochemistry. 2006 Jul 11;45(27):8341-9. PMID:16819833 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Protegrin

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